(data stored in SCRATCH zone)

SWISSPROT: Q3KJ60_PSEPF

ID   Q3KJ60_PSEPF            Unreviewed;      1317 AA.
AC   Q3KJ60;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 113.
DE   RecName: Full=Bifunctional protein PutA {ECO:0000256|PIRNR:PIRNR000197};
DE   Includes:
DE     RecName: Full=Proline dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
DE              EC=1.5.5.2 {ECO:0000256|PIRNR:PIRNR000197};
DE     AltName: Full=Proline oxidase {ECO:0000256|PIRNR:PIRNR000197};
DE   Includes:
DE     RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
DE              Short=P5C dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
DE              EC=1.2.1.88 {ECO:0000256|PIRNR:PIRNR000197};
DE     AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR000197};
GN   OrderedLocusNames=Pfl01_0452 {ECO:0000313|EMBL:ABA72196.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72196.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72196.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72196.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Oxidizes proline to glutamate for use as a carbon and
CC       nitrogen source. {ECO:0000256|PIRNR:PIRNR000197}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC         glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000197};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a
CC         quinol + H(+); Xref=Rhea:RHEA:23784, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17388, ChEBI:CHEBI:24646, ChEBI:CHEBI:60039,
CC         ChEBI:CHEBI:132124; EC=1.5.5.2;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000197};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000197};
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 1/2.
CC       {ECO:0000256|PIRNR:PIRNR000197}.
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 2/2.
CC       {ECO:0000256|PIRNR:PIRNR000197}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC       dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000197}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the proline
CC       dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000197}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000094; ABA72196.1; -; Genomic_DNA.
DR   RefSeq; WP_011332118.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0452; -.
DR   EnsemblBacteria; ABA72196; ABA72196; Pfl01_0452.
DR   KEGG; pfo:Pfl01_0452; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG0506; LUCA.
DR   eggNOG; COG4230; LUCA.
DR   HOGENOM; HOG000253911; -.
DR   KO; K13821; -.
DR   OMA; VRIYAPV; -.
DR   BioCyc; PFLU205922:G1G4S-457-MONOMER; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1220.10; -; 1.
DR   Gene3D; 1.20.5.550; -; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR013321; Arc_rbn_hlx_hlx.
DR   InterPro; IPR025703; Bifunct_PutA.
DR   InterPro; IPR005933; Delta1-pyrroline-5-COlate_DH-3.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR041349; PRODH.
DR   InterPro; IPR024090; PRODH_PutA_dom_I.
DR   InterPro; IPR024089; PRODH_PutA_dom_I/II.
DR   InterPro; IPR024082; PRODH_PutA_dom_II.
DR   InterPro; IPR002872; Proline_DH_dom.
DR   InterPro; IPR010985; Ribbon_hlx_hlx.
DR   Pfam; PF00171; Aldedh; 1.
DR   Pfam; PF01619; Pro_dh; 1.
DR   Pfam; PF14850; Pro_dh-DNA_bdg; 1.
DR   Pfam; PF18327; PRODH; 1.
DR   PIRSF; PIRSF000197; Bifunct_PutA; 1.
DR   SUPFAM; SSF47598; SSF47598; 1.
DR   SUPFAM; SSF51730; SSF51730; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   SUPFAM; SSF81935; SSF81935; 1.
DR   TIGRFAMs; TIGR01238; D1pyr5carbox3; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJ60.
DR   SWISS-2DPAGE; Q3KJ60.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   DNA-binding {ECO:0000256|PIRNR:PIRNR000197,
KW   ECO:0000256|SAAS:SAAS00993492}; FAD {ECO:0000256|PIRNR:PIRNR000197};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR000197};
KW   NAD {ECO:0000256|PIRNR:PIRNR000197};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000197,
KW   ECO:0000313|EMBL:ABA72196.1};
KW   Proline metabolism {ECO:0000256|PIRNR:PIRNR000197};
KW   Repressor {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription {ECO:0000256|PIRNR:PIRNR000197};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR000197}.
FT   DOMAIN       87    134       PRODH. {ECO:0000259|Pfam:PF18327}.
FT   DOMAIN      146    257       Pro_dh-DNA_bdg. {ECO:0000259|Pfam:
FT                                PF14850}.
FT   DOMAIN      268    567       Pro_dh. {ECO:0000259|Pfam:PF01619}.
FT   DOMAIN      656   1105       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   ACT_SITE    881    881       {ECO:0000256|PIRSR:PIRSR000197-1}.
FT   ACT_SITE    915    915       {ECO:0000256|PIRSR:PIRSR000197-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU10008}.
SQ   SEQUENCE   1317 AA;  142591 MW;  5921E396110F8E91 CRC64;
     MATTTLGVKL DDPTRERLKA AATSIDRTPH WLIKQAIFNY LEKLEGGATL TELNGLTAKD
     ADDAGEVHTD HAHQCFLEFA ESILPQSVLR ASITAAYRRP EPEVVPMLIE QARLPAPMAE
     ATNKLAATIA EKLRNQKSAG GRAGIVQGLL QEFSLSSQEG VALMCLAEAL LRIPDKGTRD
     ALIRDKISTG NWQPHLGNSP SLFVNAATWG LLLTGKLVST HNEAGLTSSL SRIIGKSGEP
     MIRKGVDMAM RLMGEQFVTG ETIAEALANA SKFEAKGFRY SYDMLGEAAL TEHDAQKYLA
     SYEQAIHSIG KASHGRGIYE GPGISIKLSA LHPRYSRAQY ERVMDELYPR LLSLTLLAKQ
     YDIGLNIDAE EADRLELSLD LLERLCFEPQ LTGWNGIGFV IQAYQKRCPY VIDYVIDLAR
     RSRHRLMIRL VKGAYWDSEI KRAQVEGLEG YPVYTRKVYT DVSYIACARK LLSVPEVIYP
     QFATHNAHTL SAIYHIAGQN YYPGQYEFQC LHGMGEPLYE QVVGKVSEGK LNRPCRVYAP
     VGTHETLLAY LVRRLLENGA NTSFVNRIAD QSVSIQELVA DPVAQIEQMA TVEGGFGLPH
     PRIPLPRDLY GSERANSAGI DMANEHRLAS LSCALLATAH NNWKAAPMLG CASSNEAPAP
     VLNPSDLRDV VGHVQEATVE DVDNAIQCAL NAAPIWQATP PAERAAILER AADLMEGEIQ
     PLMGLLAREA GKTFANAIAE VREAVDFLRY YAVQARNDFS NDAHRPLGPV VCISPWNFPL
     AIFSGQVAAA LAAGNPVLAK PAEQTPLVAA QAVRLLLEAG IPEGVLQLLP GRGETVGAGL
     VGDERVKGVM FTGSTEVARL LQRNIAGRLD NQGRPIPLIA ETGGQNAMIV DSSALTEQVV
     IDVVSSAFDS AGQRCSALRV LCLQEDSADR VIEMLKGAMA ESRLGNPERL SVDIGPVIDA
     EAKAGIEKHI QGMRDKGRNV YQVAIADTEE VKRGTFVMPT LIELESFDEL QREIFGPVLH
     VVRYKRKEID QLIAQINASG YGLTLGVHTR IDETIAKVID NVNAGNVYVN RNIVGAVVGV
     QPFGGEGLSG TGPKAGGPLY LYRLLSTRPT DAIEQSFARA DAAVAPDVRL RDAMSKPLTA
     LKAWADSNKF ADLSTLCVQY AAQSQSGITR VLAGPTGEKN SYAILPREHV LCLADIEGDL
     LTQLAAVLAV GGSAVWPESD TSKALFARLP KEIQARIKLV SDWNKDDVVF DAVLHHGHSD
     QLRAVCQQIA KRAGAIVGVQ GLSQGETNIA LERLVIERAL SVNTAAAGGN ASLMTIG
//

If you have problems or comments...

PBIL Back to PBIL home page